Crystal structure of an Xrcc4–DNA ligase IV complex

@article{Sibanda2001CrystalSO,
  title={Crystal structure of an Xrcc4–DNA ligase IV complex},
  author={Bancinyane Lynn Sibanda and Susan E. Critchlow and Jake Begun and Xue Yuan Pei and Stephen P. Jackson and Tom L. Blundell and Luca Pellegrini},
  journal={Nature Structural Biology},
  year={2001},
  volume={8},
  pages={1015-1019}
}
A complex of two proteins, Xrcc4 and DNA ligase IV, plays a fundamental role in DNA non-homologous end joining (NHEJ), a cellular function required for double-strand break repair and V(D)J recombination. Here we report the crystal structure of human Xrcc4 bound to a polypeptide that corresponds to the DNA ligase IV sequence linking its two BRCA1 C-terminal (BRCT) domains. In the complex, a single ligase chain binds asymmetrically to an Xrcc4 dimer. The helical tails of Xrcc4 undergo a… CONTINUE READING
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